Abstract
There have been remarkable developments in the methodology for protein structure analysis over the past few decades. Currently, single-wavelength anomalous diffraction phasing of a selenomethionyl derivative (Se-SAD) is used as a general method for determining protein structure, while the sulfur single-wavelength anomalous diffraction method (S-SAD) using native protein is evolving as a next-generation method. In this paper, we look back on the early applications of multi-wavelength anomalous diffraction phasing of a selenomethionyl derivative (Se-MAD) and introduce the study of ribosomal proteins as an example of the comprehensive analysis that took place in the 1990s. Furthermore, we refer to the current state of development of the S-SAD method as well as automatic structure determination.
